175224-23-4Relevant articles and documents
Thionoglycine as a multifunctional spectroscopic reporter of screw-sense preference in helical foldamers
De Poli, Matteo,Clayden, Jonathan
, p. 836 - 843 (2014)
A single thionoglycine (glycine thioamide, -HNCH2C(S)-) residue inserted into a peptide foldamer provides both a pair of germinal protons for use as a 1H NMR stereochemical probe and a chromophore giving rise to a well defined Cotton
Induction of unexpected left-handed helicity by an N-terminal L -amino acid in an otherwise achiral peptide chain
Brown, Robert A.,Marcelli, Tommaso,Depoli, Matteo,Sola, Jordi,Clayden, Jonathan
supporting information; experimental part, p. 1395 - 1399 (2012/03/27)
Peptide helices containing L-amino acids are typically right-handed. Exceptions are peptide helices containing the achiral amino acids 2-aminoisobutyric acid and glycine with a single chiral amino acid at the Nterminus. These helices are left-handed when the N-terminal residue is a common tertiary proteinogenic amino acid, such as L-valine (see picture, left), but right-handed when the N-terminal residue is the quaternary amino acid L-α-methylvaline (right). Copyright
Peptide Helices as Rigid Molecular Rulers: A Conformational Study of Isotactic Homopeptides from α-Methyl-α-isopropylglycine, n
Polese, Alessandra,Formaggio, Fernando,Crisma, Marco,Valle, Giovanni,Toniolo, Claudio,et al.
, p. 1104 - 1111 (2007/10/03)
Terminally blocked, isotactic homopeptides from the sterically demanding α-methylvaline of general formula Y-n-O-t-Bu (Y = Z, pBrBz, Ac; n = 2-8) have been prepared step-by-step in solution and fully characterized.The conformations preferred i